Structural transitions in model beta-sheet tapes

Giovanni Bellesia, Maxim V. Fedorov, Edward G. Timoshenko

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

We present a molecular-scale simulation study of the structural transitions between helicoidal, helical, and tubular geometries in supramolecular beta-sheet tapes. Such geometries have been observed in different self-assembled amyloid systems (based on either natural or synthetic peptides) for which the beta-sheet tapes represent the simplest fibrillar aggregates. A coarse-grained model for the beta-sheet tapes is proposed, with chiral degrees of freedom and asymmetrical chemical properties, which provides a quantitative characterization of the structural transitions. A quantitative connection is established between the molecular properties and the elastic parameters of the supramolecular tapes. (c) 2008 American Institute of Physics.

LanguageEnglish
Article number195105
Pages-
Number of pages7
JournalJournal of Chemical Physics
Volume128
Issue number19
DOIs
Publication statusPublished - 12 May 2008

Fingerprint

Tapes
tapes
Geometry
molecular properties
geometry
Amyloid
chemical properties
Chemical properties
peptides
Physics
degrees of freedom
Peptides
physics
simulation

Keywords

  • amphiphilic assemblies
  • molecular dynamics
  • helical ribbons
  • peptide
  • origin
  • proteins
  • forces

Cite this

Bellesia, Giovanni ; Fedorov, Maxim V. ; Timoshenko, Edward G. / Structural transitions in model beta-sheet tapes. In: Journal of Chemical Physics. 2008 ; Vol. 128, No. 19. pp. -.
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Structural transitions in model beta-sheet tapes. / Bellesia, Giovanni; Fedorov, Maxim V.; Timoshenko, Edward G.

In: Journal of Chemical Physics, Vol. 128, No. 19, 195105, 12.05.2008, p. -.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Structural transitions in model beta-sheet tapes

AU - Bellesia, Giovanni

AU - Fedorov, Maxim V.

AU - Timoshenko, Edward G.

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AB - We present a molecular-scale simulation study of the structural transitions between helicoidal, helical, and tubular geometries in supramolecular beta-sheet tapes. Such geometries have been observed in different self-assembled amyloid systems (based on either natural or synthetic peptides) for which the beta-sheet tapes represent the simplest fibrillar aggregates. A coarse-grained model for the beta-sheet tapes is proposed, with chiral degrees of freedom and asymmetrical chemical properties, which provides a quantitative characterization of the structural transitions. A quantitative connection is established between the molecular properties and the elastic parameters of the supramolecular tapes. (c) 2008 American Institute of Physics.

KW - amphiphilic assemblies

KW - molecular dynamics

KW - helical ribbons

KW - peptide

KW - origin

KW - proteins

KW - forces

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